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Antioxidant Activity of Soy Protein Hydrolysates in a Liposomal System
Author(s) -
PeñtaRamos E.A.,
Xiong Y.L.
Publication year - 2002
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.2002.tb08844.x
Subject(s) - papain , tbars , hydrolysate , chemistry , hydrolysis , antioxidant , chymotrypsin , oxidizing agent , proteases , trypsin , chromatography , liposome , lipid oxidation , pepsin , soy protein , enzymatic hydrolysis , thiobarbituric acid , enzyme , biochemistry , lipid peroxidation , organic chemistry
Native and heated soy protein isolate was hydrolyzed with 3 purified (pepsin, papain, and chymotrypsin) and 3 crude (Alcalase®, Protamex TM , and Flavourzyme TM ) proteases. The hydrolysates were incubated (37 °C, 1 h) with a liposome‐oxidizing system (50 μM FeCl 3 /0.1 mM ascorbate, pH 7.0) to test antioxidant activities by determining the concentrations of TBARS. Degree of hydrolysis of SPI hydrolysates ranged from 1.7 to 20.6%. Both hydrolyzed and nonhydrolyzed SPI decreased TBARS (by 28 to 65%), except for papain‐hydrolyzed samples. Samples of chymotrypsin‐ and Flavourzyme‐hydrolyzed (0.5 h) preheated SPI had the greatest inhibitory effect on lipid oxidation.